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[PMID]:28470519
[Au] Autor:Smolina N; Bruton J; Kostareva A; Sejersen T
[Ad] Endereço:Karolinska Institutet, Stockholm, Sweden. natalia.smolina@ki.se.
[Ti] Título:Assaying Mitochondrial Respiration as an Indicator of Cellular Metabolism and Fitness.
[So] Source:Methods Mol Biol;1601:79-87, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial respiration is the most important generator of cellular energy under most circumstances. It is a process of energy conversion of substrates into ATP. The Seahorse equipment allows measuring oxygen consumption rate (OCR) in living cells and estimates key parameters of mitochondrial respiration in real-time mode. Through use of mitochondrial inhibitors, four key mitochondrial respiration parameters can be measured: basal, ATP production-linked, maximal, and proton leak-linked OCR. This approach requires application of mitochondrial inhibitors-oligomycin to block ATP synthase, FCCP-to make the inner mitochondrial membrane permeable for protons and allow maximum electron flux through the electron transport chain, and rotenone and antimycin A-to inhibit complexes I and III, respectively. This chapter describes the protocol of OCR assessment in the culture of primary myotubes obtained upon satellite cell fusion.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Bioensaio/instrumentação
Mitocôndrias/metabolismo
Fosforilação Oxidativa
Consumo de Oxigênio
[Mh] Termos MeSH secundário: Animais
Antimicina A/farmacologia
Carbonil Cianeto p-Trifluormetoxifenil Hidrazona/farmacologia
Respiração Celular
Sobrevivência Celular
Complexo I de Transporte de Elétrons/antagonistas & inibidores
Complexo III da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Camundongos
Mitocôndrias/efeitos dos fármacos
Fibras Musculares Esqueléticas/efeitos dos fármacos
Fibras Musculares Esqueléticas/metabolismo
Oligomicinas/farmacologia
Cultura Primária de Células
Ionóforos de Próton/farmacologia
Rotenona/farmacologia
Células Satélites de Músculo Esquelético/efeitos dos fármacos
Células Satélites de Músculo Esquelético/metabolismo
Desacopladores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligomycins); 0 (Proton Ionophores); 0 (Uncoupling Agents); 03L9OT429T (Rotenone); 370-86-5 (Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone); 642-15-9 (Antimycin A); 8L70Q75FXE (Adenosine Triphosphate); EC 1.10.2.2 (Electron Transport Complex III); EC 1.6.5.3 (Electron Transport Complex I)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6960-9_7


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[PMID]:29227076
[Au] Autor:Danylovych HV
[Ti] Título:Evaluation of functioning of mitochondrial electron transport chain with NADH and FAD autofluorescence
[So] Source:Ukr Biochem J;88(1):31-43, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:We prove the feasibility of evaluation of mitochondrial electron transport chain function in isolated mitochondria of smooth muscle cells of rats from uterus using fluorescence of NADH and FAD coenzymes. We found the inversely directed changes in FAD and NADH fluorescence intensity under normal functioning of mitochondrial electron transport chain. The targeted effect of inhibitors of complex I, III and IV changed fluorescence of adenine nucleotides. Rotenone (5 µM) induced rapid increase in NADH fluorescence due to inhibition of complex I, without changing in dynamics of FAD fluorescence increase. Antimycin A, a complex III inhibitor, in concentration of 1 µg/ml caused sharp increase in NADH fluorescence and moderate increase in FAD fluorescence in comparison to control. NaN3 (5 mM), a complex IV inhibitor, and CCCP (10 µM), a protonophore, caused decrease in NADH and FAD fluorescence. Moreover, all the inhibitors caused mitochondria swelling. NO donors, e.g. 0.1 mM sodium nitroprusside and sodium nitrite similarly to the effects of sodium azide. Energy-dependent Ca2+ accumulation in mitochondrial matrix (in presence of oxidation substrates and Mg-ATP2- complex) is associated with pronounced drop in NADH and FAD fluorescence followed by increased fluorescence of adenine nucleotides, which may be primarily due to Ca2+- dependent activation of dehydrogenases of citric acid cycle. Therefore, the fluorescent signal of FAD and NADH indicates changes in oxidation state of these nucleotides in isolated mitochondria, which may be used to assay the potential of effectors of electron transport chain.
[Mh] Termos MeSH primário: Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Complexo I de Transporte de Elétrons/metabolismo
Flavina-Adenina Dinucleotídeo/química
Mitocôndrias/metabolismo
NAD/química
[Mh] Termos MeSH secundário: Animais
Antimicina A/farmacologia
Cálcio/metabolismo
Carbonil Cianeto m-Clorofenil Hidrazona/farmacologia
Fracionamento Celular
Transporte de Elétrons/efeitos dos fármacos
Complexo I de Transporte de Elétrons/antagonistas & inibidores
Complexo III da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Complexo IV da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Feminino
Flavina-Adenina Dinucleotídeo/metabolismo
Mitocôndrias/efeitos dos fármacos
Miócitos de Músculo Liso/efeitos dos fármacos
Miócitos de Músculo Liso/metabolismo
Miométrio/efeitos dos fármacos
Miométrio/metabolismo
NAD/metabolismo
Nitroprussiato/farmacologia
Imagem Óptica
Ratos
Rotenona/farmacologia
Azida Sódica/farmacologia
Nitrito de Sódio/farmacologia
Desacopladores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Uncoupling Agents); 03L9OT429T (Rotenone); 0U46U6E8UK (NAD); 146-14-5 (Flavin-Adenine Dinucleotide); 169D1260KM (Nitroprusside); 555-60-2 (Carbonyl Cyanide m-Chlorophenyl Hydrazone); 642-15-9 (Antimycin A); 968JJ8C9DV (Sodium Azide); EC 1.10.2.2 (Electron Transport Complex III); EC 1.6.5.3 (Electron Transport Complex I); EC 1.9.3.1 (Electron Transport Complex IV); M0KG633D4F (Sodium Nitrite); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.031


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[PMID]:28450391
[Au] Autor:Korge P; Calmettes G; John SA; Weiss JN
[Ad] Endereço:From the UCLA Cardiovascular Research Laboratory and the Departments of Medicine (Cardiology) and Physiology, David Geffen School of Medicine at UCLA, Los Angeles, California 90095.
[Ti] Título:Reactive oxygen species production induced by pore opening in cardiac mitochondria: The role of complex III.
[So] Source:J Biol Chem;292(24):9882-9895, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent evidence has implicated succinate-driven reverse electron transport (RET) through complex I as a major source of damaging reactive oxygen species (ROS) underlying reperfusion injury after prolonged cardiac ischemia. However, this explanation may be incomplete, because RET on reperfusion is self-limiting and therefore transient. RET can only generate ROS when mitochondria are well polarized, and it ceases when permeability transition pores (PTP) open during reperfusion. Because prolonged ischemia/reperfusion also damages electron transport complexes, we investigated whether such damage could lead to ROS production after PTP opening has occurred. Using isolated cardiac mitochondria, we demonstrate a novel mechanism by which antimycin-inhibited complex III generates significant amounts of ROS in the presence of Mg and NAD and the absence of exogenous substrates upon inner membrane pore formation by alamethicin or Ca -induced PTP opening. We show that H O production under these conditions is related to Mg -dependent NADH generation by malic enzyme. H O production is blocked by stigmatellin, indicating its origin from complex III, and by piericidin, demonstrating the importance of NADH-related ubiquinone reduction for ROS production under these conditions. For maximal ROS production, the rate of NADH generation has to be equal or below that of NADH oxidation, as further increases in [NADH] elevate ubiquinol-related complex III reduction beyond the optimal range for ROS generation. These results suggest that if complex III is damaged during ischemia, PTP opening may result in succinate/malate-fueled ROS production from complex III due to activation of malic enzyme by increases in matrix [Mg ], [NAD ], and [ADP].
[Mh] Termos MeSH primário: Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Malato Desidrogenase/metabolismo
Mitocôndrias Cardíacas/metabolismo
Espécies Reativas de Oxigênio/agonistas
[Mh] Termos MeSH secundário: Difosfato de Adenosina/metabolismo
Alameticina/farmacologia
Animais
Antimicina A/análogos & derivados
Antimicina A/farmacologia
Biocatálise/efeitos dos fármacos
Sinalização do Cálcio/efeitos dos fármacos
Complexo III da Cadeia de Transporte de Elétrons/antagonistas & inibidores
Ativação Enzimática/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
Peróxido de Hidrogênio/metabolismo
Ionóforos/farmacologia
Magnésio/metabolismo
Malato Desidrogenase/química
Mitocôndrias Cardíacas/química
Mitocôndrias Cardíacas/efeitos dos fármacos
NAD/metabolismo
Oxirredução
Polienos/farmacologia
Porosidade/efeitos dos fármacos
Piridinas/farmacologia
Coelhos
Espécies Reativas de Oxigênio/metabolismo
Ubiquinona/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Ionophores); 0 (Polyenes); 0 (Pyridines); 0 (Reactive Oxygen Species); 0U46U6E8UK (NAD); 11118-72-2 (antimycin); 1339-63-5 (Ubiquinone); 27061-78-5 (Alamethicin); 61D2G4IYVH (Adenosine Diphosphate); 642-15-9 (Antimycin A); 8VT513UJ9R (piericidin A); 91682-96-1 (stigmatellin); BBX060AN9V (Hydrogen Peroxide); EC 1.1.1.37 (Malate Dehydrogenase); EC 1.10.2.2 (Electron Transport Complex III); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.768317


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[PMID]:28554565
[Au] Autor:Jezek J; Engstová H; Jezek P
[Ad] Endereço:Department No. 75, Institute of Physiology, Academy of Sciences, Vídenská 1083, Prague 14220, Czech Republic. Electronic address: jezekj6@rowan.edu.
[Ti] Título:Antioxidant mechanism of mitochondria-targeted plastoquinone SkQ1 is suppressed in aglycemic HepG2 cells dependent on oxidative phosphorylation.
[So] Source:Biochim Biophys Acta;1858(9):750-762, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Previously suggested antioxidant mechanisms for mitochondria-targeted plastoquinone SkQ1 included: i) ion-pairing of cationic SkQ1 with free fatty acid anions resulting in uncoupling; ii) SkQ1H ability to interact with lipoperoxyl radical; iii) interference with electron flow at the inner ubiquinone (Q) binding site of Complex III (Q ), involving the reduction of SkQ1 to SkQ1H by ubiquinol. We elucidated SkQ1 antioxidant properties by confocal fluorescence semi-quantification of mitochondrial superoxide (J ) and cytosolic H O (J ) release rates in HepG2 cells. Only in glycolytic cells, SkQ1 prevented the rotenone-induced enhancement of J and J but not basal releases without rotenone. The effect ceased in glutaminolytic aglycemic cells, in which the redox parameter NAD(P)H/FAD increased after rotenone in contrast to its decrease in glycolytic cells. Autofluorescence decay indicated decreased NADPH/NADH ratios with rotenone in both metabolic modes. SkQ1 did not increase cell respiration and diminished J established high by antimycin or myxothiazol but not by stigmatellin. The revealed SkQ1 antioxidant modes reflect its reduction to SkQ1H at Complex I I or Complex III Q site. Both reductions diminish electron diversions to oxygen thus attenuating superoxide formation. Resulting SkQ1H oxidizes back to SkQ1at the second (flavin) Complex I site, previously indicated for MitoQ . Regeneration proceeds only at lower NAD(P)H/FAD in glycolytic cells. In contrast, cyclic SkQ1 reduction/SkQ1H oxidation does not substantiate antioxidant activity in intact cells in the absence of oxidative stress (neither pro-oxidant activity, representing a great advantage). A targeted delivery to oxidative-stressed tissues is suggested for the effective antioxidant therapy based on SkQ1.
[Mh] Termos MeSH primário: Antioxidantes/farmacologia
Mitocôndrias/efeitos dos fármacos
Fosforilação Oxidativa
Plastoquinona/análogos & derivados
[Mh] Termos MeSH secundário: Antimicina A/análogos & derivados
Antimicina A/farmacologia
Complexo I de Transporte de Elétrons/metabolismo
Complexo III da Cadeia de Transporte de Elétrons/metabolismo
Flavina-Adenina Dinucleotídeo/metabolismo
Glicólise
Células Hep G2
Seres Humanos
Metacrilatos/farmacologia
Mitocôndrias/metabolismo
NAD/metabolismo
Oxirredução
Estresse Oxidativo
Plastoquinona/farmacologia
Polienos/farmacologia
Rotenona/farmacologia
Superóxidos/metabolismo
Tiazóis/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (10-(6'-plastoquinonyl)decyltriphenylphosphonium); 0 (Antioxidants); 0 (Methacrylates); 0 (Polyenes); 0 (Thiazoles); 03L9OT429T (Rotenone); 0U46U6E8UK (NAD); 11062-77-4 (Superoxides); 11118-72-2 (antimycin); 146-14-5 (Flavin-Adenine Dinucleotide); 642-15-9 (Antimycin A); 76706-55-3 (myxothiazol); 91682-96-1 (stigmatellin); EC 1.10.2.2 (Electron Transport Complex III); EC 1.6.5.3 (Electron Transport Complex I); OAC30J69CN (Plastoquinone)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170531
[St] Status:MEDLINE


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[PMID]:28438607
[Au] Autor:Boudoures AL; Saben J; Drury A; Scheaffer S; Modi Z; Zhang W; Moley KH
[Ad] Endereço:Center for Reproductive and Health Sciences, Washington University in St. Louis, St. Louis, MO, USA.
[Ti] Título:Obesity-exposed oocytes accumulate and transmit damaged mitochondria due to an inability to activate mitophagy.
[So] Source:Dev Biol;426(1):126-138, 2017 06 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondria are the most prominent organelle in the oocyte. Somatic cells maintain a healthy population of mitochondria by degrading damaged mitochondria via mitophagy, a specialized autophagy pathway. However, evidence from previous work investigating the more general macroautophagy pathway in oocytes suggests that mitophagy may not be active in the oocyte. This would leave the vast numbers of mitochondria - poised to be inherited by the offspring - vulnerable to damage. Here we test the hypothesis that inactive mitophagy in the oocyte underlies maternal transmission of dysfunctional mitochondria. To determine whether oocytes can complete mitophagy, we used either CCCP or AntimycinA to depolarize mitochondria and trigger mitophagy. After depolarization, we did not detect co-localization of mitochondria with autophagosomes and mitochondrial DNA copy number remained unchanged, indicating the non-functional mitochondrial population was not removed. To investigate the impact of an absence of mitophagy in oocytes with damaged mitochondria on offspring mitochondrial function, we utilized in vitro fertilization of high fat high sugar (HF/HS)-exposed oocytes, which have lower mitochondrial membrane potential and damaged mitochondria. Here, we demonstrate that blastocysts generated from HF/HS oocytes have decreased mitochondrial membrane potential, lower metabolites involved in ATP generation, and accumulation of PINK1, a mitophagy marker protein. This mitochondrial phenotype in the blastocyst mirrors the phenotype we show in HF/HS exposed oocytes. Taken together, these data suggest that the mechanisms governing oocyte mitophagy are fundamentally distinct from those governing somatic cell mitophagy and that the absence of mitophagy in the setting of HF/HS exposure contributes to the oocyte-to-blastocyst transmission of dysfunctional mitochondria.
[Mh] Termos MeSH primário: Autofagia/fisiologia
DNA Mitocondrial/genética
Dosagem de Genes/genética
Potencial da Membrana Mitocondrial/fisiologia
Mitocôndrias/patologia
Degradação Mitocondrial/fisiologia
Oócitos/metabolismo
[Mh] Termos MeSH secundário: Animais
Antimicina A/toxicidade
Células Cultivadas
Feminino
Dosagem de Genes/efeitos dos fármacos
Hidrazonas/toxicidade
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Obesidade/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Hydrazones); 14046-96-9 (carbonyl 3-chlorophenylhydrazone); 642-15-9 (Antimycin A)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170426
[St] Status:MEDLINE


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[PMID]:28306143
[Au] Autor:Raini G; Sharet R; Herrero M; Atzmon A; Shenoy A; Geiger T; Elroy-Stein O
[Ad] Endereço:Department of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
[Ti] Título:Mutant eIF2B leads to impaired mitochondrial oxidative phosphorylation in vanishing white matter disease.
[So] Source:J Neurochem;141(5):694-707, 2017 Jun.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Eukaryotic translation initiation factor 2B (eIF2B) is a master regulator of protein synthesis under normal and stress conditions. Mutations in any of the five genes encoding its subunits lead to vanishing white matter (VWM) disease, a recessive genetic deadly illness caused by progressive loss of white matter in the brain. In this study we used fibroblasts, which are not involved in the disease, to demonstrate the involvement of eIF2B in mitochondrial function and abundance. Mass spectrometry of total proteome of mouse embryonic fibroblasts (MEFs) isolated from Eif2b5 mice revealed unbalanced stoichiometry of proteins involved in oxidative phosphorylation and of mitochondrial translation machinery components, among others. Mutant MEFs exhibit 55% decrease in oxygen consumption rate per mtDNA content and 47% increase in mitochondrial abundance (p < 0.005), reflecting adaptation to energy requirements. A more robust eIF2B-associated oxidative respiration deficiency was found in mutant primary astrocytes, which exhibit > 3-fold lower ATP-linked respiration per cell despite a 2-fold increase in mtDNA content (p < 0.03). The 2-fold increase in basal and stimulated glycolysis in mutant astrocytes (p ≤ 0.03), but not in MEFs, demonstrates their higher energetic needs and further explicates their involvement in the disease. The data demonstrate the critical role of eIF2B in tight coordination of expression from nuclear and mitochondrial genomes and illuminates the importance of mitochondrial function in VWM pathology. Further dissection of the signaling network associated with eIF2B function will help generating therapeutic strategies for VWM disease and possibly other neurodegenerative disorders.
[Mh] Termos MeSH primário: Astrócitos/ultraestrutura
Fator de Iniciação 2B em Eucariotos/genética
Mitocôndrias/genética
Mutação/genética
Fosforilação Oxidativa
Consumo de Oxigênio/genética
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Antimicina A/farmacologia
Astrócitos/efeitos dos fármacos
Astrócitos/fisiologia
Carbonil Cianeto p-Trifluormetoxifenil Hidrazona/farmacologia
Ciclo Celular/efeitos dos fármacos
Ciclo Celular/genética
Tamanho Celular
Células Cultivadas
Cloranfenicol/farmacologia
Fator de Iniciação 2B em Eucariotos/metabolismo
Feminino
Fibroblastos/efeitos dos fármacos
Fibroblastos/imunologia
Fibroblastos/ultraestrutura
Antígenos de Histocompatibilidade/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Mitocôndrias/fisiologia
Fosforilação Oxidativa/efeitos dos fármacos
Consumo de Oxigênio/efeitos dos fármacos
Fosforilação/efeitos dos fármacos
Fosforilação/genética
Biossíntese de Proteínas/efeitos dos fármacos
Biossíntese de Proteínas/genética
Inibidores da Síntese de Proteínas/farmacologia
Ionóforos de Próton/farmacologia
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eukaryotic Initiation Factor-2B); 0 (Histocompatibility Antigens); 0 (Protein Synthesis Inhibitors); 0 (Proton Ionophores); 0 (Reactive Oxygen Species); 370-86-5 (Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone); 642-15-9 (Antimycin A); 66974FR9Q1 (Chloramphenicol)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.14024


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[PMID]:28167700
[Au] Autor:Zhang X; Ivanova A; Vandepoele K; Radomiljac J; Van de Velde J; Berkowitz O; Willems P; Xu Y; Ng S; Van Aken O; Duncan O; Zhang B; Storme V; Chan KX; Vaneechoutte D; Pogson BJ; Van Breusegem F; Whelan J; De Clercq I
[Ad] Endereço:Key Laboratory of Plant Resources Conservation and Sustainable Utilization, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou 510650, China (X.Z).
[Ti] Título:The Transcription Factor MYB29 Is a Regulator of .
[So] Source:Plant Physiol;173(3):1824-1843, 2017 03.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plants sense and integrate a variety of signals from the environment through different interacting signal transduction pathways that involve hormones and signaling molecules. Using ( ) gene expression as a model system of retrograde or stress signaling between mitochondria and the nucleus, MYB DOMAIN PROTEIN29 (MYB29) was identified as a negative regulator ( [ ] mutant) in a genetic screen of Arabidopsis ( ). mutants have increased levels of AOX1a transcript and protein compared to wild type after induction with antimycin A. A variety of genes previously associated with the mitochondrial stress response also display enhanced transcript abundance, indicating that RAO7/MYB29 negatively regulates mitochondrial stress responses in general. Meta-analysis of hormone-responsive marker genes and identification of downstream transcription factor networks revealed that MYB29 functions in the complex interplay of ethylene, jasmonic acid, salicylic acid, and reactive oxygen species signaling by regulating the expression of various ETHYLENE RESPONSE FACTOR and WRKY transcription factors. Despite an enhanced induction of mitochondrial stress response genes, / mutants displayed an increased sensitivity to combined moderate light and drought stress. These results uncover interactions between mitochondrial retrograde signaling and the regulation of glucosinolate biosynthesis, both regulated by RAO7/MYB29. This common regulator can explain why perturbation of the mitochondrial function leads to transcriptomic responses overlapping with responses to biotic stress.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Regulação da Expressão Gênica de Plantas/genética
Proteínas Mitocondriais/genética
Oxirredutases/genética
Proteínas de Plantas/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Antimicina A/farmacologia
Arabidopsis/enzimologia
Arabidopsis/metabolismo
Proteínas de Arabidopsis/metabolismo
Núcleo Celular/genética
Núcleo Celular/metabolismo
Perfilação da Expressão Gênica/métodos
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Ontologia Genética
Redes Reguladoras de Genes
Immunoblotting
Mitocôndrias/genética
Mitocôndrias/metabolismo
Proteínas Mitocondriais/metabolismo
Mutação
Oxirredutases/metabolismo
Proteínas de Plantas/metabolismo
Plantas Geneticamente Modificadas
Regiões Promotoras Genéticas/genética
Ligação Proteica
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transdução de Sinais/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Mitochondrial Proteins); 0 (Myb29 protein, Arabidopsis); 0 (Plant Proteins); 0 (Transcription Factors); 642-15-9 (Antimycin A); EC 1.- (Oxidoreductases); EC 1.- (alternative oxidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170208
[St] Status:MEDLINE
[do] DOI:10.1104/pp.16.01494


  8 / 2847 MEDLINE  
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[PMID]:28103219
[Au] Autor:Georgakopoulos ND; Wells G; Campanella M
[Ad] Endereço:Department of Comparative Biomedical Sciences, The Royal Veterinary College, University of London, London, UK.
[Ti] Título:The pharmacological regulation of cellular mitophagy.
[So] Source:Nat Chem Biol;13(2):136-146, 2017 Jan 19.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Small molecules are pharmacological tools of considerable value for dissecting complex biological processes and identifying potential therapeutic interventions. Recently, the cellular quality-control process of mitophagy has attracted considerable research interest; however, the limited availability of suitable chemical probes has restricted our understanding of the molecular mechanisms involved. Current approaches to initiate mitophagy include acute dissipation of the mitochondrial membrane potential (ΔΨ ) by mitochondrial uncouplers (for example, FCCP/CCCP) and the use of antimycin A and oligomycin to impair respiration. Both approaches impair mitochondrial homeostasis and therefore limit the scope for dissection of subtle, bioenergy-related regulatory phenomena. Recently, novel mitophagy activators acting independently of the respiration collapse have been reported, offering new opportunities to understand the process and potential for therapeutic exploitation. We have summarized the current status of mitophagy modulators and analyzed the available chemical tools, commenting on their advantages, limitations and current applications.
[Mh] Termos MeSH primário: Antimicina A/farmacologia
Mitocôndrias/efeitos dos fármacos
Degradação Mitocondrial/efeitos dos fármacos
Oligomicinas/farmacologia
[Mh] Termos MeSH secundário: Antimicina A/química
Seres Humanos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Mitocôndrias/metabolismo
Mitocôndrias/patologia
Estrutura Molecular
Oligomicinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Oligomycins); 642-15-9 (Antimycin A)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170504
[Lr] Data última revisão:
170504
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2287


  9 / 2847 MEDLINE  
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[PMID]:28026135
[Au] Autor:Shan J; Chen L; Lu K
[Ad] Endereço:Department of Anesthesia, Affiliated Hospital of Weifang Medical University, Weifang, Shandong Province, China.
[Ti] Título:Protective effects of trans-caryophyllene on maintaining osteoblast function.
[So] Source:IUBMB Life;69(1):22-29, 2017 Jan.
[Is] ISSN:1521-6551
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Age-related osteoblast dysfunction is the main cause of age-related bone loss. Trans-caryophyllene (TC) is an important constituent of the essential oils derived from several species of medicinal plants. In this study, we investigated the effects of TC on osteoblast function in osteoblastic MC3T3-E1 cells. The results indicate that TC caused a significant elevation in collagen content, alkaline phosphatase activity, osteocalcin production, and mineralization, which are the four markers that account for the various stages of osteoblastic differentiation. In addition, pretreatment with TC prior to antimycin A exposure significantly reduced antimycin A-induced cell damage by attenuating cell death, preventing the release of reactive oxygen species and impeding osteoblast dysfunction. TC has been shown to be an agonist of the cannabinoid type 2 receptor (CB2R), and the effects of TC on osteocalcin secretion and matrix mineralization were abolished in MC3T3E1 cells transfected with CB2R siRNA. Our findings that TC promotes the formation of a mineralized extracellular matrix help to elucidate the role of CB2 signaling in the formation of bone and the maintenance of normal bone mass. © 2016 IUBMB Life, 69(1):22-29, 2017.
[Mh] Termos MeSH primário: Diferenciação Celular/efeitos dos fármacos
Óleos Voláteis/administração & dosagem
Osteoblastos/efeitos dos fármacos
Osteoporose/tratamento farmacológico
Sesquiterpenos/administração & dosagem
[Mh] Termos MeSH secundário: Células 3T3-L1
Animais
Antimicina A/toxicidade
Colágeno/biossíntese
Matriz Extracelular/efeitos dos fármacos
Seres Humanos
Camundongos
Óleos Voláteis/química
Osteoporose/induzido quimicamente
Osteoporose/patologia
Espécies Reativas de Oxigênio/metabolismo
Sesquiterpenos/química
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oils, Volatile); 0 (Reactive Oxygen Species); 0 (Sesquiterpenes); 642-15-9 (Antimycin A); 9007-34-5 (Collagen); BHW853AU9H (caryophyllene)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE
[do] DOI:10.1002/iub.1584


  10 / 2847 MEDLINE  
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[PMID]:28012971
[Au] Autor:Peters E; Schirris T; van Asbeck AH; Gerretsen J; Eymael J; Ashikov A; Adjobo-Hermans MJ; Russel F; Pickkers P; Masereeuw R
[Ad] Endereço:Department of Intensive Care Medicine, Radboud University Medical Center, PO Box 9101, Internal Mailbox 710, 6500 HB Nijmegen, The Netherlands; Department of Pharmacology and Toxicology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, PO Box 9101, Internal Mailbox 7
[Ti] Título:Effects of a human recombinant alkaline phosphatase during impaired mitochondrial function in human renal proximal tubule epithelial cells.
[So] Source:Eur J Pharmacol;796:149-157, 2017 Feb 05.
[Is] ISSN:1879-0712
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Sepsis-associated acute kidney injury is a multifactorial syndrome in which inflammation and renal microcirculatory dysfunction play a profound role. Subsequently, renal tubule mitochondria reprioritize cellular functions to prevent further damage. Here, we investigated the putative protective effects of human recombinant alkaline phosphatase (recAP) during inhibition of mitochondrial respiration in conditionally immortalized human proximal tubule epithelial cells (ciPTEC). Full inhibition of mitochondrial oxygen consumption was obtained after 24h antimycin A treatment, which did not affect cell viability. While recAP did not affect the antimycin A-induced decreased oxygen consumption and increased hypoxia-inducible factor-1α or adrenomedullin gene expression levels, the antimycin A-induced increase of pro-inflammatory cytokines IL-6 and IL-8 was attenuated. Antimycin A tended to induce the release of detrimental purines ATP and ADP, which reached statistical significance when antimycin A was co-incubated with lipopolysaccharide, and were completely converted into cytoprotective adenosine by recAP. As the adenosine A receptor was up-regulated after antimycin A exposure, an adenosine A receptor knockout ciPTEC cell line was generated in which recAP still provided protection. Together, recAP did not affect oxygen consumption but attenuated the inflammatory response during impaired mitochondrial function, an effect suggested to be mediated by dephosphorylating ATP and ADP into adenosine.
[Mh] Termos MeSH primário: Fosfatase Alcalina/farmacologia
Células Epiteliais/citologia
Células Epiteliais/efeitos dos fármacos
Túbulos Renais Proximais/citologia
Mitocôndrias/efeitos dos fármacos
Proteínas Recombinantes/farmacologia
[Mh] Termos MeSH secundário: Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Antimicina A/farmacologia
Linhagem Celular
Células Epiteliais/metabolismo
Seres Humanos
Mitocôndrias/metabolismo
Fosforilação/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 61D2G4IYVH (Adenosine Diphosphate); 642-15-9 (Antimycin A); 8L70Q75FXE (Adenosine Triphosphate); EC 3.1.3.1 (Alkaline Phosphatase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161226
[St] Status:MEDLINE



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